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    J Mol Biol. 1999 Aug 20;291(3):651-60.

    Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus.

    Isupov MN, Fleming TM, Dalby AR, Crowhurst GS, Bourne PC, Littlechild JA.

    Schools of Chemistry and Biological Sciences, University of Exeter, Stocker Road, Exeter, EX4 4QD, UK.

    The enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from the archaea shows low sequence identity (16-20%) with its eubacterial and eukaryotic counterparts. The crystal structure of the apo GAPDH from Sulfolobus solfataricus has been determined by multiple isomorphous replacement at 2.05 A resolution. The enzyme has several differences in secondary structure when compared with eubacterial GAPDHs, with an overall increase in the number of alpha-helices. There is a relocation of the active-site residues within the catalytic domain of the enzyme. The thermostability of the S. solfataricus enzyme can be attributed to a combination of an ion pair cluster and an intrasubunit disulphide bond. Copyright 1999 Academic Press.

    PMID: 10448043 [PubMed - indexed for MEDLINE]

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